Articles de revues sur le sujet « Metalloenzimi »
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Höcker, Birte. "A metalloenzyme reloaded." Nature Chemical Biology 8, no. 3 (2012): 224–25. http://dx.doi.org/10.1038/nchembio.800.
Texte intégralYou, Jing-Song, Xiao-Qi Yu, Xiao-Yu Su, et al. "Hydrolytic metalloenzyme models." Journal of Molecular Catalysis A: Chemical 202, no. 1-2 (2003): 17–22. http://dx.doi.org/10.1016/s1381-1169(03)00199-7.
Texte intégralDong, Steven D., and Ronald Breslow. "Bifunctional cyclodextrin metalloenzyme mimics." Tetrahedron Letters 39, no. 51 (1998): 9343–46. http://dx.doi.org/10.1016/s0040-4039(98)02160-1.
Texte intégralHadianawala, Murtuza, and Bhaskar Datta. "Design and development of sulfonylurea derivatives as zinc metalloenzyme modulators." RSC Advances 6, no. 11 (2016): 8923–29. http://dx.doi.org/10.1039/c5ra27341b.
Texte intégralKwon, Hanna, Jaswir Basran, Juliette M. Devos, et al. "Visualizing the protons in a metalloenzyme electron proton transfer pathway." Proceedings of the National Academy of Sciences 117, no. 12 (2020): 6484–90. http://dx.doi.org/10.1073/pnas.1918936117.
Texte intégralValdez, Crystal E., Amanda Morgenstern, Mark E. Eberhart, and Anastassia N. Alexandrova. "Predictive methods for computational metalloenzyme redesign – a test case with carboxypeptidase A." Physical Chemistry Chemical Physics 18, no. 46 (2016): 31744–56. http://dx.doi.org/10.1039/c6cp02247b.
Texte intégralDoerr, Allison. "Metalloenzyme structures in a shot." Nature Methods 10, no. 4 (2013): 287. http://dx.doi.org/10.1038/nmeth.2428.
Texte intégralLancaster, Kyle M. "Revving up an artificial metalloenzyme." Science 361, no. 6407 (2018): 1071–72. http://dx.doi.org/10.1126/science.aau7754.
Texte intégralStoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.
Texte intégralVallee, B. L. "Zinc metalloenzyme structure and function." Journal of Inorganic Biochemistry 36, no. 3-4 (1989): 299. http://dx.doi.org/10.1016/0162-0134(89)84446-0.
Texte intégralMarchal, Iris. "Microbial metalloenzyme boosts cellulose breakdown." Nature Biotechnology 43, no. 3 (2025): 301. https://doi.org/10.1038/s41587-025-02615-x.
Texte intégralJackl, Moritz K., Hyeonglim Seo, Johannes Karges, Mark Kalaj, and Seth M. Cohen. "Salicylate metal-binding isosteres as fragments for metalloenzyme inhibition." Chemical Science 13, no. 7 (2022): 2128–36. http://dx.doi.org/10.1039/d1sc06011b.
Texte intégralEhudin, Melanie A., Andrew W. Schaefer, Suzanne M. Adam, et al. "Influence of intramolecular secondary sphere hydrogen-bonding interactions on cytochrome c oxidase inspired low-spin heme–peroxo–copper complexes." Chemical Science 10, no. 10 (2019): 2893–905. http://dx.doi.org/10.1039/c8sc05165h.
Texte intégralLi, Yinghao, Mingpan Cheng, Jingya Hao, Changhao Wang, Guoqing Jia, and Can Li. "Terpyridine–Cu(ii) targeting human telomeric DNA to produce highly stereospecific G-quadruplex DNA metalloenzyme." Chemical Science 6, no. 10 (2015): 5578–85. http://dx.doi.org/10.1039/c5sc01381j.
Texte intégralSchneider, Camille R., and Hannah S. Shafaat. "An internal electron reservoir enhances catalytic CO2 reduction by a semisynthetic enzyme." Chemical Communications 52, no. 64 (2016): 9889–92. http://dx.doi.org/10.1039/c6cc03901d.
Texte intégralJohnson, Heather C., Shaoguang Zhang, Anna Fryszkowska, et al. "Biocatalytic oxidation of alcohols using galactose oxidase and a manganese(iii) activator for the synthesis of islatravir." Organic & Biomolecular Chemistry 19, no. 7 (2021): 1620–25. http://dx.doi.org/10.1039/d0ob02395g.
Texte intégralSmith, Meghan A., Sean H. Majer, Avery C. Vilbert, and Kyle M. Lancaster. "Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460." Chemical Science 10, no. 13 (2019): 3756–64. http://dx.doi.org/10.1039/c9sc00195f.
Texte intégralReed, Christopher J., Quan N. Lam, Evan N. Mirts, and Yi Lu. "Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling." Chemical Society Reviews 50, no. 4 (2021): 2486–539. http://dx.doi.org/10.1039/d0cs01297a.
Texte intégralZubi, Yasmine S., Bingqing Liu, Yifan Gu, Dipankar Sahoo, and Jared C. Lewis. "Controlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineering." Chemical Science 13, no. 5 (2022): 1459–68. http://dx.doi.org/10.1039/d1sc05792h.
Texte intégralTAGAKI, Waichiro, and Kenji OGINO. "Proteolytic Metalloenzyme Models in Micellar Systems." Journal of Japan Oil Chemists' Society 39, no. 10 (1990): 744–52. http://dx.doi.org/10.5650/jos1956.39.10_744.
Texte intégralMayer, Clemens, Dennis G. Gillingham, Thomas R. Ward, and Donald Hilvert. "An artificial metalloenzyme for olefin metathesis." Chemical Communications 47, no. 44 (2011): 12068. http://dx.doi.org/10.1039/c1cc15005g.
Texte intégralBersellini, Manuela, and Gerard Roelfes. "A metal ion regulated artificial metalloenzyme." Dalton Transactions 46, no. 13 (2017): 4325–30. http://dx.doi.org/10.1039/c7dt00533d.
Texte intégralDay, Joshua A., and Seth M. Cohen. "Investigating the Selectivity of Metalloenzyme Inhibitors." Journal of Medicinal Chemistry 56, no. 20 (2013): 7997–8007. http://dx.doi.org/10.1021/jm401053m.
Texte intégralFunk, Michael A. "Itaconate brings metalloenzyme to a halt." Science 366, no. 6465 (2019): 583.13–585. http://dx.doi.org/10.1126/science.366.6465.583-m.
Texte intégralArmstrong, Richard N. "Mechanistic Diversity in a Metalloenzyme Superfamily†." Biochemistry 39, no. 45 (2000): 13625–32. http://dx.doi.org/10.1021/bi001814v.
Texte intégralKoder, Ronald L., Bernard Everson, Lei Zhang, Jonathan Preston, and Emma Bjerkefeldt. "Optimizing Protein Dynamics in Metalloenzyme Design." Biophysical Journal 112, no. 3 (2017): 193a. http://dx.doi.org/10.1016/j.bpj.2016.11.1072.
Texte intégralHaeggström, Jesper Z., Anders Wetterholm, Robert Shapiro, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: A zinc metalloenzyme." Biochemical and Biophysical Research Communications 172, no. 3 (1990): 965–70. http://dx.doi.org/10.1016/0006-291x(90)91540-9.
Texte intégralGrubmeyer, Charles, Marios Skiadopoulos, and Alan E. Senior. "l-Histidinol dehydrogenase, a Zn2+-metalloenzyme." Archives of Biochemistry and Biophysics 272, no. 2 (1989): 311–17. http://dx.doi.org/10.1016/0003-9861(89)90224-5.
Texte intégralOkamoto, Yasunori, and Thomas R. Ward. "Cross-Regulation of an Artificial Metalloenzyme." Angewandte Chemie 129, no. 34 (2017): 10290–94. http://dx.doi.org/10.1002/ange.201702181.
Texte intégralDong, Steven D., and Ronald Breslow. "ChemInform Abstract: Bifunctional Cyclodextrin Metalloenzyme Mimics." ChemInform 30, no. 10 (2010): no. http://dx.doi.org/10.1002/chin.199910229.
Texte intégralOkamoto, Yasunori, and Thomas R. Ward. "Cross-Regulation of an Artificial Metalloenzyme." Angewandte Chemie International Edition 56, no. 34 (2017): 10156–60. http://dx.doi.org/10.1002/anie.201702181.
Texte intégralMafy, Noushaba Nusrat, Dorothea B. Hudson, and Emily L. Que. "Control of metalloenzyme activity using photopharmacophores." Coordination Chemistry Reviews 499 (January 2024): 215485. http://dx.doi.org/10.1016/j.ccr.2023.215485.
Texte intégralKarges, Johannes, Ryjul W. Stokes, and Seth M. Cohen. "Photorelease of a metal-binding pharmacophore from a Ru(ii) polypyridine complex." Dalton Transactions 50, no. 8 (2021): 2757–65. http://dx.doi.org/10.1039/d0dt04290k.
Texte intégralZhang, Yaoyao, Weiying Wang, Wenqin Fu, et al. "Titanium(iv)-folded single-chain polymeric nanoparticles as artificial metalloenzyme for asymmetric sulfoxidation in water." Chemical Communications 54, no. 68 (2018): 9430–33. http://dx.doi.org/10.1039/c8cc05590d.
Texte intégralLionetto, Maria Giulia. "Carbonic Anhydrase and Biomarker Research: New Insights." International Journal of Molecular Sciences 24, no. 11 (2023): 9687. http://dx.doi.org/10.3390/ijms24119687.
Texte intégralSchneider, Camille R., Anastasia C. Manesis, Michael J. Stevenson, and Hannah S. Shafaat. "A photoactive semisynthetic metalloenzyme exhibits complete selectivity for CO2 reduction in water." Chemical Communications 54, no. 37 (2018): 4681–84. http://dx.doi.org/10.1039/c8cc01297k.
Texte intégralHorch, Marius, Ana Filipa Pinto, Maria Andrea Mroginski, Miguel Teixeira, Peter Hildebrandt, and Ingo Zebger. "Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase." RSC Adv. 4, no. 96 (2014): 54091–95. http://dx.doi.org/10.1039/c4ra11976b.
Texte intégralCheng, Wenting, Jiehua Ma, Yongchen Zhang, et al. "Bio-inspired construction of a semi-artificial enzyme complex for detecting histone acetyltransferases activity." Analyst 145, no. 2 (2020): 613–18. http://dx.doi.org/10.1039/c9an01896d.
Texte intégralMus, Florence, Alexander B. Alleman, Natasha Pence, Lance C. Seefeldt, and John W. Peters. "Exploring the alternatives of biological nitrogen fixation." Metallomics 10, no. 4 (2018): 523–38. http://dx.doi.org/10.1039/c8mt00038g.
Texte intégralLi, Yinghao, Changhao Wang, Jingya Hao, Mingpan Cheng, Guoqing Jia, and Can Li. "Higher-order human telomeric G-quadruplex DNA metalloenzyme catalyzed Diels–Alder reaction: an unexpected inversion of enantioselectivity modulated by K+ and NH4+ ions." Chemical Communications 51, no. 67 (2015): 13174–77. http://dx.doi.org/10.1039/c5cc05215g.
Texte intégralDick, Benjamin L., Ashay Patel, and Seth M. Cohen. "Effect of heterocycle content on metal binding isostere coordination." Chemical Science 11, no. 26 (2020): 6907–14. http://dx.doi.org/10.1039/d0sc02717k.
Texte intégralHarty, Matthew L., Amar Nath Sharma, and Stephen L. Bearne. "Catalytic properties of the metal ion variants of mandelate racemase reveal alterations in the apparent electrophilicity of the metal cofactor." Metallomics 11, no. 3 (2019): 707–23. http://dx.doi.org/10.1039/c8mt00330k.
Texte intégralD’Alonzo, Daniele, Maria De Fenza, Vincenzo Pavone, Angela Lombardi, and Flavia Nastri. "Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase." International Journal of Molecular Sciences 24, no. 9 (2023): 8058. http://dx.doi.org/10.3390/ijms24098058.
Texte intégralAlbareda, Marta, Agnès Rodrigue, Belén Brito, et al. "Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake." Metallomics 7, no. 4 (2015): 691–701. http://dx.doi.org/10.1039/c4mt00298a.
Texte intégralZambrano, Gerardo, Alina Sekretareva, Daniele D'Alonzo, et al. "Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme." RSC Advances 12, no. 21 (2022): 12947–56. http://dx.doi.org/10.1039/d2ra00811d.
Texte intégralHerrero, Christian, Annamaria Quaranta, Rémy Ricoux, et al. "Oxidation catalysis via visible-light water activation of a [Ru(bpy)3]2+ chromophore BSA–metallocorrole couple." Dalton Transactions 45, no. 2 (2016): 706–10. http://dx.doi.org/10.1039/c5dt04158a.
Texte intégralLaureanti, Joseph A., Qiwen Su, and Wendy J. Shaw. "A protein scaffold enables hydrogen evolution for a Ni-bisdiphosphine complex." Dalton Transactions 50, no. 43 (2021): 15754–59. http://dx.doi.org/10.1039/d1dt03295j.
Texte intégralHonarmand Ebrahimi, Kourosh. "A unifying view of the broad-spectrum antiviral activity of RSAD2 (viperin) based on its radical-SAM chemistry." Metallomics 10, no. 4 (2018): 539–52. http://dx.doi.org/10.1039/c7mt00341b.
Texte intégralZhang, Lu, Yajun Yang, Ying Yang, and Zhiyan Xiao. "Discovery of Novel Metalloenzyme Inhibitors Based on Property Characterization: Strategy and Application for HDAC1 Inhibitors." Molecules 29, no. 5 (2024): 1096. http://dx.doi.org/10.3390/molecules29051096.
Texte intégralKim, Sung-Kun, Cynthe L. Sims, Susan E. Wozniak, Stephanie H. Drude, Dustin Whitson, and Robert W. Shaw. "Antibiotic Resistance in Bacteria: Novel Metalloenzyme Inhibitors." Chemical Biology & Drug Design 74, no. 4 (2009): 343–48. http://dx.doi.org/10.1111/j.1747-0285.2009.00879.x.
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